VP2_POVLY
ID VP2_POVLY Reviewed; 356 AA.
AC P04011; Q84182;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 99.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS B-lymphotropic polyomavirus (LPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; unclassified Polyomaviridae.
OX NCBI_TaxID=332091;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998001; DOI=10.1016/0042-6822(85)90108-4;
RA Pawlita M., Clad A., zur Hausen H.;
RT "Complete DNA sequence of lymphotropic papovavirus: prototype of a new
RT species of the polyomavirus genus.";
RL Virology 143:196-211(1985).
RN [2]
RP SEQUENCE REVISION.
RA Pawlita M., Clad A., zur Hausen H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3495678; DOI=10.7883/yoken1952.39.151;
RA Furuno A., Kanda T., Yoshiike K.;
RT "Monkey B-lymphotropic papovavirus genome: the entire DNA sequence and
RT variable regions.";
RL Jpn. J. Med. Sci. Biol. 39:151-161(1986).
RN [4]
RP REVIEW.
RX PubMed=19157478; DOI=10.1016/j.virol.2008.12.021;
RA Neu U., Stehle T., Atwood W.J.;
RT "The Polyomaviridae: Contributions of virus structure to our understanding
RT of virus receptors and infectious entry.";
RL Virology 384:389-399(2009).
CC -!- FUNCTION: Isoform VP2 is a structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Participates in host
CC cell receptor binding together with VP1. Following virus endocytosis
CC and trafficking to the endoplasmic reticulum, VP2 and VP3 form
CC oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Plays a role in virion assembly within the
CC nucleus in particular through a DNA-binding domain located in the C-
CC terminal region. A N-terminal myristoylation suggests a scaffold
CC function for virion assembly. The viral progenies exit the cells by
CC lytic release (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Isoform VP3]: Structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Following virus
CC endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3
CC form oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Isoform VP3 plays a role in virion assembly
CC within the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Isoform VP2 forms homooligomers, and heterooligomers with VP3
CC in the endoplasmic reticulum membrane. Isoform VP2 interacts (via D1
CC domain) with VP1. Isoform VP3 interacts (via D1 domain) with VP1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host
CC endoplasmic reticulum. Host endoplasmic reticulum membrane
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host
CC endoplasmic reticulum. Host endoplasmic reticulum membrane
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P04011-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P04011-2; Sequence=VSP_018920;
CC Name=VP1;
CC IsoId=P04010-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform VP2]: Produced by alternative splicing of the
CC late mRNA.
CC -!- MISCELLANEOUS: [Isoform VP3]: Produced by alternative initiation at
CC Met-120 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; K02562; AAA47060.2; -; Genomic_DNA.
DR EMBL; K02562; AAA47061.2; -; Genomic_DNA.
DR EMBL; M30540; AAA47069.1; -; Genomic_DNA.
DR PIR; A03634; VVVP2L.
DR RefSeq; NP_848005.2; NC_004763.2.
DR GeneID; 1494440; -.
DR KEGG; vg:1494440; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR InterPro; IPR001070; Polyoma_coat_VP2.
DR Pfam; PF00761; Polyoma_coat2; 1.
DR PIRSF; PIRSF003377; Polyoma_coat2; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Alternative splicing; Capsid protein; DNA-binding;
KW Host endoplasmic reticulum; Host membrane; Host nucleus; Late protein;
KW Lipoprotein; Membrane; Myristate; Transmembrane; Transmembrane helix;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..356
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039213"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 233..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..303
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 308..354
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 312..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 320..326
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 236..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018920"
SQ SEQUENCE 356 AA; 39536 MW; 0B6AFE7177CF530A CRC64;
MGGVLSLLFN ISEIAAELSL STGFTVDAIL TGEAFAAVST EAAWLIEIEA VDLAGLSTLE
ALSLTGLTTE QFSLLSAIPT ALNNAIGIGV FFQTVSGASA VVAAGVTTFG YSKEVPVVNM
ALVPWFPQVD YLFPGFTSFS YYLNAVLDWG ESLFHAVGRE VWRHLMRQAT LQIGQATRAV
AVRSTNELSH TLAQIAENAR WALTSGPVHI YSSVQDYYRY LPARNPIQLR QEYRNRGEPP
PSRADFEYQE NREGQRARRE LGYDEPRSGQ YVEHYTAPGG AHQRVTQDWM LPLILGLYGD
ITPTWEVELN KLEKEEDGPS KKKARRSMQK NMPYSRSRPQ APSKRRSRGA RSKNRA
